Methyltransferases excised from trans-AT polyketide synthases operate on N-acetylcysteamine-bound substrates.
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Domain Organization and Active Site Architecture of a Polyketide Synthase C-methyltransferasePolyketide stereocontrol: a study in chemical biology.Elucidation of the Stereospecificity of C-Methyltransferases from trans-AT Polyketide Synthases.Engineering modular polyketide synthases for production of biofuels and industrial chemicals.Chemistry of a Unique Polyketide-like Synthase.
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Methyltransferases excised from trans-AT polyketide synthases operate on N-acetylcysteamine-bound substrates.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 15 June 2016
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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Methyltransferases excised fro ...... ylcysteamine-bound substrates.
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Methyltransferases excised fro ...... ylcysteamine-bound substrates.
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type
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Methyltransferases excised fro ...... ylcysteamine-bound substrates.
@en
Methyltransferases excised fro ...... ylcysteamine-bound substrates.
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Methyltransferases excised fro ...... ylcysteamine-bound substrates.
@en
Methyltransferases excised fro ...... ylcysteamine-bound substrates.
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P2093
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P356
P1476
Methyltransferases excised fro ...... ylcysteamine-bound substrates.
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Adrian T Keatinge-Clay
Bradley K Alexander
Drew T Wagner
Hannah R Manion
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P2888
P304
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10.1038/JA.2016.66
P577
2016-06-15T00:00:00Z